Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes-Reference-Cited by-同舟云学术

Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes

Published:2010-12-02 Issue:3 Volume:24 Page:301-309
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Park J. H.,Dias C. A. O.,Lee S. B.,Valentini S. R.,Sokabe M.,Fraser C. S.,Park M. H.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/24/3/301/4491396/gzq110.pdf

Reference47 articles.

1. Expression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexes

2. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.

3. Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70 S Ribosome

4. The role of hypusine depletion in cytostasis induced by S-adenosyl-l-methionine decarboxylase inhibition: new evidence provided by 1-methylspermidine and 1,12-dimethylspermine

5. Mutational analyses of human eIF5A-1 - identification of amino acid residues critical for eIF5A activity and hypusine modification

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